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- W2791799892 endingPage "283" @default.
- W2791799892 startingPage "283" @default.
- W2791799892 abstract "Intracellular synthesis, folding, trafficking and degradation of proteins are controlled and integrated by proteostasis. The frequency of protein misfolding disorders in the human population, e.g., in Alzheimer's disease (AD), is increasing due to the aging population. AD treatment options are limited to symptomatic interventions that at best slow-down disease progression. The key biochemical change in AD is the excessive accumulation of per-se non-toxic and soluble amyloid peptides (Aβ(1-37/44), in the intracellular and extracellular space, that alters proteostasis and triggers Aβ modification (e.g., by reactive oxygen species (ROS)) into toxic intermediate, misfolded soluble Aβ peptides, Aβ dimers and Aβ oligomers. The toxic intermediate Aβ products aggregate into progressively less toxic and less soluble protofibrils, fibrils and senile plaques. This review focuses on peptides that inhibit toxic Aβ oligomerization, Aβ aggregation into fibrils, or stabilize Aβ peptides in non-toxic oligomers, and discusses their potential for AD treatment." @default.
- W2791799892 created "2018-03-29" @default.
- W2791799892 creator A5005410846 @default.
- W2791799892 date "2018-01-30" @default.
- W2791799892 modified "2023-10-17" @default.
- W2791799892 title "Peptides as Potential Therapeutics for Alzheimer’s Disease" @default.
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